Xanthomonas oryzae pv. oryzae TALE proteins recruit OsTFIIAγ1 to compensate for the absence of OsTFIIAγ5 in bacterial blight in rice

Authors

Wenxiu Ma, Shanghai Jiao Tong University/Key Laboratory of Urban Agriculture by Ministry of Agriculture
Lifang Zou, Shanghai Jiao Tong University/Key Laboratory of Urban Agriculture by Ministry of Agriculture
Zhiyuan Ji, Shanghai Jiao Tong University/Key Laboratory of Urban Agriculture by Ministry of Agriculture
Xiameng Xu, Shanghai Jiao Tong University/Key Laboratory of Urban Agriculture by Ministry of Agriculture
Zhengyin Xu, Shanghai Jiao Tong University/Key Laboratory of Urban Agriculture by Ministry of Agriculture
YangYang Yang, Shanghai Jiao Tong University/Key Laboratory of Urban Agriculture by Ministry of Agriculture
James R. Alfano, University of Nebraska at Lincoln & Shanghai Jiao Tong University/Key Laboratory of Urban Agriculture by Ministry of AgricultureFollow

ORCID IDs

http://orcid.org/0000-0003-1979-2880

Date of this Version

2018

Citation

2018 THE AUTHORS. MOLECULAR PLANT PATHOLOGY PUBLISHED BY BRITISH SOCIETY FOR PLANT PATHOLOGY AND JOHN WILEY & SONS LTD

Comments

Molecular Plant Pathology (2018) 19(10), 2248–2262 DOI : 10.1111/mpp.12696

Abstract

Xanthomonas oryzae pv. oryzae (Xoo), the causal agent of bacterial blight (BB) of rice, uses transcription activator-like effectors (TALEs) to interact with the basal transcription factor gamma subunit OsTFIIAγ5 (Xa5) and activates the transcription of host genes. However, how OsTFIIAγ1, the other OsTFIIAγ protein, functions in the presence of TALEs remains unclear. In this study, we show that OsTFIIAγ1 plays a compensatory role in the absence of Xa5. The expression of OsTFIIAγ1, which is activated by TALE PthXo7, increases the expression of host genes targeted by avirulent and virulent TALEs. Defective OsTFIIAγ1 rice lines show reduced expression of the TALE-targeted susceptibility (S) genes, OsSWEET11 and OsSWEET14, which results in increased BB resistance. Selected TALEs (PthXo1, AvrXa7 and AvrXa27) were evaluated for interactions with OsTFIIAγ1, Xa5 and xa5 (naturally occurring mutant form of Xa5) using biomolecular fluorescence complementation (BiFC) and microscale thermophoresis (MST). BiFC and MST demonstrated that the three TALEs bind Xa5 and OsTFIIAγ1 with a stronger affinity than xa5. These results provide insights into the complex roles of OsTFIIAγ1 and OsTFIIAγ5 in TALE-mediated host gene transcription.